메뉴 건너뛰기




Volumn 11, Issue 22, 2011, Pages 4346-4367

Coordination of carbon fixation and nitrogen metabolism in Salicornia europaea under salinity: Comparative proteomic analysis on chloroplast proteins

Author keywords

Carbon fixation; Chloroplast proteomics; Halophyte; Nitrogen metabolism; Photosynthesis; Plant proteomics

Indexed keywords

ARTICLE; CARBON FIXATION; CHLOROPLAST; HALOPHYTE; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NITROGEN METABOLISM; NONHUMAN; PHOTOACTIVATION; PHOTOSYNTHESIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEOMICS; SALICORNIA EUROPAEA; SALINITY; TWO DIMENSIONAL GEL ELECTROPHORESIS; ULTRASTRUCTURE;

EID: 80055109077     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100054     Document Type: Article
Times cited : (63)

References (88)
  • 2
    • 0027811507 scopus 로고
    • Physiological processes limiting plant-growth in saline soils - some dogmas and hypotheses
    • Munns, R., Physiological processes limiting plant-growth in saline soils - some dogmas and hypotheses. Plant Cell Environ. 1993, 16, 15-24.
    • (1993) Plant Cell Environ. , vol.16 , pp. 15-24
    • Munns, R.1
  • 3
    • 0028814720 scopus 로고
    • The significance of a two-phase growth response to salinity in wheat and barley
    • Munns, R., Schachtman, D. P., Condon, A. G., The significance of a two-phase growth response to salinity in wheat and barley. Aust. J. Plant Physiol. 1995, 22, 561-569.
    • (1995) Aust. J. Plant Physiol. , vol.22 , pp. 561-569
    • Munns, R.1    Schachtman, D.P.2    Condon, A.G.3
  • 4
    • 1142281833 scopus 로고    scopus 로고
    • Improving crop salt tolerance
    • Flowers, T. J., Improving crop salt tolerance. J. Exp. Bot. 2004, 55, 307-319.
    • (2004) J. Exp. Bot. , vol.55 , pp. 307-319
    • Flowers, T.J.1
  • 7
    • 0035213385 scopus 로고    scopus 로고
    • Plant salt tolerance
    • Zhu, J. K., Plant salt tolerance. Trends Plant Sci. 2001, 6, 66-71.
    • (2001) Trends Plant Sci. , vol.6 , pp. 66-71
    • Zhu, J.K.1
  • 8
    • 0036999615 scopus 로고    scopus 로고
    • Salt and drought stress signal transduction in plants
    • Zhu, J. K., Salt and drought stress signal transduction in plants. Annu. Rev. Plant Biol. 2002, 53, 247-273.
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 247-273
    • Zhu, J.K.1
  • 9
    • 0038325577 scopus 로고    scopus 로고
    • A salt-tolerant cultivar of wheat maintains photosynthetic activity by suppressing sodium uptake
    • Muranaka, S., Shimizu, K., Kato, M., A salt-tolerant cultivar of wheat maintains photosynthetic activity by suppressing sodium uptake. Photosynthetica 2002, 40, 509-515.
    • (2002) Photosynthetica , vol.40 , pp. 509-515
    • Muranaka, S.1    Shimizu, K.2    Kato, M.3
  • 10
    • 0001059498 scopus 로고
    • Photosynthesis and ion content of leaves and isolated-chloroplasts of salt-stressed spinach
    • Robinson, S. P., Downton, W. J. S., Millhouse, J. A., Photosynthesis and ion content of leaves and isolated-chloroplasts of salt-stressed spinach. Plant Physiol. 1983, 73, 238-242.
    • (1983) Plant Physiol. , vol.73 , pp. 238-242
    • Robinson, S.P.1    Downton, W.J.S.2    Millhouse, J.A.3
  • 11
    • 0001952187 scopus 로고
    • Photosynthetic and stomatal responses of the grey mangrove, Avicennia-marina, to transient salinity conditions
    • Ball, M. C., Farquhar, G. D., Photosynthetic and stomatal responses of the grey mangrove, Avicennia-marina, to transient salinity conditions. Plant Physiol. 1984, 74, 7-11.
    • (1984) Plant Physiol. , vol.74 , pp. 7-11
    • Ball, M.C.1    Farquhar, G.D.2
  • 12
    • 77949296073 scopus 로고    scopus 로고
    • Effects of salt stress on photosynthesis, PSII photochemistry and thermal energy dissipation in leaves of two corn (Zea mays L.) varieties
    • Hichem, H., Naceur, E. A., Mounir, D., Effects of salt stress on photosynthesis, PSII photochemistry and thermal energy dissipation in leaves of two corn (Zea mays L.) varieties. Photosynthetica 2009, 47, 517-526.
    • (2009) Photosynthetica , vol.47 , pp. 517-526
    • Hichem, H.1    Naceur, E.A.2    Mounir, D.3
  • 13
    • 70450171298 scopus 로고    scopus 로고
    • Photosynthetic response of salt-tolerant and sensitive soybean varieties
    • Lu, K. X., Cao, B. H., Feng, X. P., He, Y. et al., Photosynthetic response of salt-tolerant and sensitive soybean varieties. Photosynthetica 2009, 47, 381-387.
    • (2009) Photosynthetica , vol.47 , pp. 381-387
    • Lu, K.X.1    Cao, B.H.2    Feng, X.P.3    He, Y.4
  • 14
    • 72149119072 scopus 로고    scopus 로고
    • Chlorophyll a fluorescence study revealing effects of high salt stress on Photosystem II in wheat leaves
    • Mehta, P., Jajoo, A., Mathur, S., Bharti, S., Chlorophyll a fluorescence study revealing effects of high salt stress on Photosystem II in wheat leaves. Plant Physiol. Biochem. 2010, 48, 16-20.
    • (2010) Plant Physiol. Biochem. , vol.48 , pp. 16-20
    • Mehta, P.1    Jajoo, A.2    Mathur, S.3    Bharti, S.4
  • 15
    • 60249103271 scopus 로고    scopus 로고
    • Contrasting responses of photosynthesis to salt stress in the glycophyte Arabidopsis and the halophyte Thellungiella: role of the plastid terminal oxidase as an alternative electron sink
    • Stepien, P., Johnson, G. N., Contrasting responses of photosynthesis to salt stress in the glycophyte Arabidopsis and the halophyte Thellungiella: role of the plastid terminal oxidase as an alternative electron sink. Plant Physiol. 2009, 149, 1154-1165.
    • (2009) Plant Physiol. , vol.149 , pp. 1154-1165
    • Stepien, P.1    Johnson, G.N.2
  • 16
    • 0031291308 scopus 로고    scopus 로고
    • Photosynthesis in rice under a salt stress
    • Tiwari, B. S., Bose, A., Ghosh, B., Photosynthesis in rice under a salt stress. Photosynthetica 1997, 34, 303-306.
    • (1997) Photosynthetica , vol.34 , pp. 303-306
    • Tiwari, B.S.1    Bose, A.2    Ghosh, B.3
  • 17
    • 4644327784 scopus 로고    scopus 로고
    • Pretreatment with antioxidants decreases the effects of salt stress on chloroplast ultrastructure in rice leaf segments (Oryza sativa L.)
    • Yamane, K., Rahman, S., Kawasaki, M., Taniguchi, M. et al., Pretreatment with antioxidants decreases the effects of salt stress on chloroplast ultrastructure in rice leaf segments (Oryza sativa L.). Plant Prod. Sci. 2004, 7, 292-300.
    • (2004) Plant Prod. Sci. , vol.7 , pp. 292-300
    • Yamane, K.1    Rahman, S.2    Kawasaki, M.3    Taniguchi, M.4
  • 18
    • 60449097159 scopus 로고    scopus 로고
    • Effects of salt and waterlogging stresses and their combination on leaf photosynthesis, chloroplast ATP synthesis, and antioxidant capacity in wheat
    • Zheng, C. F., Jiang, D., Liu, F. L., Dai, T. B. et al., Effects of salt and waterlogging stresses and their combination on leaf photosynthesis, chloroplast ATP synthesis, and antioxidant capacity in wheat. Plant Sci. 2009, 176, 575-582.
    • (2009) Plant Sci. , vol.176 , pp. 575-582
    • Zheng, C.F.1    Jiang, D.2    Liu, F.L.3    Dai, T.B.4
  • 19
    • 40649117642 scopus 로고    scopus 로고
    • Effect of NaCl on photosynthesis, salt accumulation and ion compartmentation in two mangrove species, Kandelia candel and Bruguiera gymnorhiza
    • Li, N. Y., Chen, S. L., Zhou, X. Y., Li, C. Y. et al., Effect of NaCl on photosynthesis, salt accumulation and ion compartmentation in two mangrove species, Kandelia candel and Bruguiera gymnorhiza. Aquat. Bot. 2008, 88, 303-310.
    • (2008) Aquat. Bot. , vol.88 , pp. 303-310
    • Li, N.Y.1    Chen, S.L.2    Zhou, X.Y.3    Li, C.Y.4
  • 20
    • 49249139258 scopus 로고    scopus 로고
    • Salinity tolerance in halophytes
    • Flowers, T. J., Colmer, T. D., Salinity tolerance in halophytes. New Phytol. 2008, 179, 945-963.
    • (2008) New Phytol. , vol.179 , pp. 945-963
    • Flowers, T.J.1    Colmer, T.D.2
  • 21
    • 77951104035 scopus 로고    scopus 로고
    • Salt stimulation of growth and photosynthesis in an extreme halophyte, Arthrocnemum macrostachyum
    • Redondo-Gomez, S., Mateos-Naranjo, E., Figueroa, M. E., Davy, A. J., Salt stimulation of growth and photosynthesis in an extreme halophyte, Arthrocnemum macrostachyum. Plant Biol. 2010, 12, 79-87.
    • (2010) Plant Biol. , vol.12 , pp. 79-87
    • Redondo-Gomez, S.1    Mateos-Naranjo, E.2    Figueroa, M.E.3    Davy, A.J.4
  • 22
    • 0041347812 scopus 로고    scopus 로고
    • Enhanced tolerance of photosynthesis against high temperature damage in salt-adapted halophyte Atriplex centralasiatica plants
    • Qiu, N., Lu, C., Enhanced tolerance of photosynthesis against high temperature damage in salt-adapted halophyte Atriplex centralasiatica plants. Plant Cell Environ. 2003, 26, 1137-1145.
    • (2003) Plant Cell Environ. , vol.26 , pp. 1137-1145
    • Qiu, N.1    Lu, C.2
  • 23
    • 0041347629 scopus 로고    scopus 로고
    • Photosynthesis, photosystem II efficiency and the xanthophyll cycle in the salt-adapted halophyte Atriplex centralasiatica
    • Qiu, N. W., Lu, Q. T., Lu, C. M., Photosynthesis, photosystem II efficiency and the xanthophyll cycle in the salt-adapted halophyte Atriplex centralasiatica. New Phytol. 2003, 159, 479-486.
    • (2003) New Phytol. , vol.159 , pp. 479-486
    • Qiu, N.W.1    Lu, Q.T.2    Lu, C.M.3
  • 26
    • 78449296002 scopus 로고    scopus 로고
    • Organelle proteomics experimental designs and analysis
    • Gatto, L., Vizcaino, J. A., Hermjako, H., Huber, W. et al., Organelle proteomics experimental designs and analysis. Proteomics 2010, 10, 3957-3969.
    • (2010) Proteomics , vol.10 , pp. 3957-3969
    • Gatto, L.1    Vizcaino, J.A.2    Hermjako, H.3    Huber, W.4
  • 27
    • 66749083834 scopus 로고    scopus 로고
    • Oxidative damage of mitochondrial proteins contributes to fruit senescence: a redox proteomics analysis
    • Qin, G. Z., Meng, X. H., Wang, Q., Tian, S. P., Oxidative damage of mitochondrial proteins contributes to fruit senescence: a redox proteomics analysis. J. Proteome Res. 2009, 8, 2449-2462.
    • (2009) J. Proteome Res. , vol.8 , pp. 2449-2462
    • Qin, G.Z.1    Meng, X.H.2    Wang, Q.3    Tian, S.P.4
  • 28
    • 39049153858 scopus 로고    scopus 로고
    • Proteomics approach to identify dehydration responsive nuclear proteins from chickpea (Cicer arietinum L.)
    • Pandey, A., Chakraborty, S., Datta, A., Chakraborty, N., Proteomics approach to identify dehydration responsive nuclear proteins from chickpea (Cicer arietinum L.). Mol. Cell. Proteomics 2008, 7, 88-107.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 88-107
    • Pandey, A.1    Chakraborty, S.2    Datta, A.3    Chakraborty, N.4
  • 29
    • 67049095501 scopus 로고    scopus 로고
    • Proteomic analysis of plasma membranes of Cyanobacterium Synechocystis sp strain PCC 6803 in response to high pH stress
    • Zhang, L. F., Yang, H. M., Cui, S. X., Hu, J. et al., Proteomic analysis of plasma membranes of Cyanobacterium Synechocystis sp strain PCC 6803 in response to high pH stress. J. Proteome Res. 2009, 8, 2892-2902.
    • (2009) J. Proteome Res. , vol.8 , pp. 2892-2902
    • Zhang, L.F.1    Yang, H.M.2    Cui, S.X.3    Hu, J.4
  • 30
    • 79955022797 scopus 로고    scopus 로고
    • Integrated proteome and metabolite analysis of the de-etiolation process in plastids from rice (Oryza sativa L.)
    • Baginsky, S., Reiland, S., Grossmann, J., Baerenfaller, K. et al., Integrated proteome and metabolite analysis of the de-etiolation process in plastids from rice (Oryza sativa L.). Proteomics 2011, 11, 1751-1763.
    • (2011) Proteomics , vol.11 , pp. 1751-1763
    • Baginsky, S.1    Reiland, S.2    Grossmann, J.3    Baerenfaller, K.4
  • 31
    • 69949107836 scopus 로고    scopus 로고
    • Short-term effects of salt exposure on the maize chloroplast protein pattern
    • Zorb, C., Herbst, R., Forreiter, C., Schubert, S., Short-term effects of salt exposure on the maize chloroplast protein pattern. Proteomics 2009, 9, 4209-4220.
    • (2009) Proteomics , vol.9 , pp. 4209-4220
    • Zorb, C.1    Herbst, R.2    Forreiter, C.3    Schubert, S.4
  • 32
    • 78650022779 scopus 로고    scopus 로고
    • Alterations in phosphoproteome under salt stress in Thellungiella roots
    • Zhou, Y. J., Gao, F., Li, X. F., Zhang, J. et al., Alterations in phosphoproteome under salt stress in Thellungiella roots. Chinese Sci. Bull. 2010, 55, 3673-3679.
    • (2010) Chinese Sci. Bull. , vol.55 , pp. 3673-3679
    • Zhou, Y.J.1    Gao, F.2    Li, X.F.3    Zhang, J.4
  • 33
    • 77952065773 scopus 로고    scopus 로고
    • Comparative proteomics of salt tolerance in Arabidopsis thaliana and Thellungiella halophila
    • Pang, Q. Y., Chen, S. X., Dai, S. J., Chen, Y. Z. et al., Comparative proteomics of salt tolerance in Arabidopsis thaliana and Thellungiella halophila. J. Proteome Res. 2010, 9, 2584-2599.
    • (2010) J. Proteome Res. , vol.9 , pp. 2584-2599
    • Pang, Q.Y.1    Chen, S.X.2    Dai, S.J.3    Chen, Y.Z.4
  • 34
    • 56349109991 scopus 로고    scopus 로고
    • Proteomic analysis of long-term salinity stress-responsive proteins in Thellungiella halophila leaves
    • Gao, F., Zhou, Y. J., Huang, L. Y., He, D. C. et al., Proteomic analysis of long-term salinity stress-responsive proteins in Thellungiella halophila leaves. Chinese Sci. Bull. 2008, 53, 3530-3537.
    • (2008) Chinese Sci. Bull. , vol.53 , pp. 3530-3537
    • Gao, F.1    Zhou, Y.J.2    Huang, L.Y.3    He, D.C.4
  • 35
    • 33646255908 scopus 로고    scopus 로고
    • Effects of salinity levels on proteome of Suaeda aegyptiaca leaves
    • Askari, H., Edqvist, J., Hajheidari, M., Kafi, M. et al., Effects of salinity levels on proteome of Suaeda aegyptiaca leaves. Proteomics 2006, 6, 2542-2554.
    • (2006) Proteomics , vol.6 , pp. 2542-2554
    • Askari, H.1    Edqvist, J.2    Hajheidari, M.3    Kafi, M.4
  • 36
    • 0023496062 scopus 로고
    • Population characteristics, growth, and survival of the halophyte Salicornia europaea
    • Ungar, I. A., Population characteristics, growth, and survival of the halophyte Salicornia europaea. Ecology 1987, 68, 569-575.
    • (1987) Ecology , vol.68 , pp. 569-575
    • Ungar, I.A.1
  • 37
    • 33750584579 scopus 로고    scopus 로고
    • Effect of photosynthetically active radiation, salinization, and type of nitrogen nutrition on growth of Salicornia europaea plants
    • Ushakova, S. A., Kovaleva, N. P., Tikhomirova, N. A., Gribovskaya, I. V. et al., Effect of photosynthetically active radiation, salinization, and type of nitrogen nutrition on growth of Salicornia europaea plants. Russian J. Plant Physiol. 2006, 53, 785-792.
    • (2006) Russian J. Plant Physiol. , vol.53 , pp. 785-792
    • Ushakova, S.A.1    Kovaleva, N.P.2    Tikhomirova, N.A.3    Gribovskaya, I.V.4
  • 38
    • 24644437332 scopus 로고    scopus 로고
    • Influence of high concentrations of mineral salts on production process and NaCl accumulation by Salicornia europaea plants as a constituent of the LSS phototroph link
    • Tikhomirova, N. A., Ushakova, S. A., Kovaleva, N. P., Gribovskaya, I. V. et al., Influence of high concentrations of mineral salts on production process and NaCl accumulation by Salicornia europaea plants as a constituent of the LSS phototroph link. Adv. Space Res. 2005, 35, 1589-1593.
    • (2005) Adv. Space Res. , vol.35 , pp. 1589-1593
    • Tikhomirova, N.A.1    Ushakova, S.A.2    Kovaleva, N.P.3    Gribovskaya, I.V.4
  • 39
    • 27844515217 scopus 로고    scopus 로고
    • Effect of NaCl concentration on productivity and mineral composition of Salicornia europaea as a potential crop for utilization NaCl in LSS
    • Ushakova, S. A., Kovaleva, N. P., Gribovskaya, T. V., Dolgushev, V. A. et al., Effect of NaCl concentration on productivity and mineral composition of Salicornia europaea as a potential crop for utilization NaCl in LSS. Adv. Space Res. 2005, 36, 1349-1353.
    • (2005) Adv. Space Res. , vol.36 , pp. 1349-1353
    • Ushakova, S.A.1    Kovaleva, N.P.2    Gribovskaya, T.V.3    Dolgushev, V.A.4
  • 40
    • 67650388759 scopus 로고    scopus 로고
    • Comparative proteomic analysis of differentially expressed proteins in shoots of Salicornia europaea under different salinity
    • Wang, X. C., Fan, P. X., Song, H. M., Chen, X. Y. et al., Comparative proteomic analysis of differentially expressed proteins in shoots of Salicornia europaea under different salinity. J. Proteome Res. 2009, 8, 3331-3345.
    • (2009) J. Proteome Res. , vol.8 , pp. 3331-3345
    • Wang, X.C.1    Fan, P.X.2    Song, H.M.3    Chen, X.Y.4
  • 41
    • 0024934011 scopus 로고
    • Photosynthesis of salt-marsh species
    • Drake, B. G., Photosynthesis of salt-marsh species. Aquat. Bot. 1989, 34, 167-180.
    • (1989) Aquat. Bot. , vol.34 , pp. 167-180
    • Drake, B.G.1
  • 42
    • 33847009860 scopus 로고    scopus 로고
    • 4 vegetation in a Northern New England salt marsh, Sprague Marsh, Phippsburg Maine
    • 4 vegetation in a Northern New England salt marsh, Sprague Marsh, Phippsburg Maine. Org. Geochem. 2007, 38, 394-403.
    • (2007) Org. Geochem. , vol.38 , pp. 394-403
    • Johnson, B.J.1    Moore, K.A.2    Lehmann, C.3    Bohlen, C.4
  • 43
    • 0000408822 scopus 로고
    • Photosynthetic pathways and the ecological distribution of the Chenopodiaceae in Israel
    • Shomerilan, A., Nissenbaum, A., Waisel, Y., Photosynthetic pathways and the ecological distribution of the Chenopodiaceae in Israel. Oecologia 1981, 48, 244-248.
    • (1981) Oecologia , vol.48 , pp. 244-248
    • Shomerilan, A.1    Nissenbaum, A.2    Waisel, Y.3
  • 44
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra, R. J., Thompson, W. A., Kriedemann, P. E., Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim. Biophys. Acta 1989, 975, 384-394.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 45
    • 44949110144 scopus 로고    scopus 로고
    • Chlorophyll fluorescence: a probe of photosynthesis in vivo
    • Baker, N. R., Chlorophyll fluorescence: a probe of photosynthesis in vivo. Annu. Rev. Plant Biol. 2008, 59, 89-113.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 89-113
    • Baker, N.R.1
  • 46
    • 0034063592 scopus 로고    scopus 로고
    • Chlorophyll fluorescence - A practical guide
    • Maxwell, K., Johnson, G. N., Chlorophyll fluorescence - A practical guide. J. Exp. Bot. 2000, 51, 659-668.
    • (2000) J. Exp. Bot. , vol.51 , pp. 659-668
    • Maxwell, K.1    Johnson, G.N.2
  • 47
    • 70449912949 scopus 로고    scopus 로고
    • An efficient method for the extraction of chloroplast proteins compatible for 2-DE and MS analysis
    • Fan, P. X., Wang, X. C., Kuang, T. Y., Li, Y. X., An efficient method for the extraction of chloroplast proteins compatible for 2-DE and MS analysis. Electrophoresis 2009, 30, 3024-3033.
    • (2009) Electrophoresis , vol.30 , pp. 3024-3033
    • Fan, P.X.1    Wang, X.C.2    Kuang, T.Y.3    Li, Y.X.4
  • 48
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford, M. M., Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 49
    • 34548119185 scopus 로고    scopus 로고
    • A modified Coomassie Brilliant Blue staining method at nanogram sensitivity compatible with proteomic analysis
    • Wang, X. C., Li, X. F., Li, Y. X., A modified Coomassie Brilliant Blue staining method at nanogram sensitivity compatible with proteomic analysis. Biotechnol. Lett. 2007, 29, 1599-1603.
    • (2007) Biotechnol. Lett. , vol.29 , pp. 1599-1603
    • Wang, X.C.1    Li, X.F.2    Li, Y.X.3
  • 50
    • 35948954213 scopus 로고    scopus 로고
    • A protein extraction method compatible with proteomic analysis for the euhalophyte Salicornia europaea
    • Wang, X. C., Li, X. F., Deng, X., Han, H. P. et al., A protein extraction method compatible with proteomic analysis for the euhalophyte Salicornia europaea. Electrophoresis 2007, 28, 3976-3987.
    • (2007) Electrophoresis , vol.28 , pp. 3976-3987
    • Wang, X.C.1    Li, X.F.2    Deng, X.3    Han, H.P.4
  • 51
    • 40749104608 scopus 로고    scopus 로고
    • Proteomic analysis of aqueous humor from patients with myopia
    • Wang, N. L., Duan, X. M., Lu, Q. J., Xue, P. et al., Proteomic analysis of aqueous humor from patients with myopia. Mol. Vis. 2008, 14, 370-377.
    • (2008) Mol. Vis. , vol.14 , pp. 370-377
    • Wang, N.L.1    Duan, X.M.2    Lu, Q.J.3    Xue, P.4
  • 52
    • 12144291195 scopus 로고    scopus 로고
    • MAPMAN: a user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes
    • Thimm, O., Blasing, O., Gibon, Y., Nagel, A. et al., MAPMAN: a user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes. Plant J. 2004, 37, 914-939.
    • (2004) Plant J. , vol.37 , pp. 914-939
    • Thimm, O.1    Blasing, O.2    Gibon, Y.3    Nagel, A.4
  • 53
    • 27244453164 scopus 로고    scopus 로고
    • Extension of the visualization tool MapMan to allow statistical analysis of arrays, display of corresponding genes, and comparison with known responses
    • Usadel, B., Nagel, A., Thimm, O., Redestig, H. et al., Extension of the visualization tool MapMan to allow statistical analysis of arrays, display of corresponding genes, and comparison with known responses. Plant Physiol. 2005, 138, 1195-1204.
    • (2005) Plant Physiol. , vol.138 , pp. 1195-1204
    • Usadel, B.1    Nagel, A.2    Thimm, O.3    Redestig, H.4
  • 55
    • 34250636225 scopus 로고    scopus 로고
    • Formation of DEG5 and DEG8 complexes and their involvement in the degradation of photodamaged photosystem II reaction center D1 protein in Arabidopsis
    • Sun, X. W., Peng, L. W., Guo, J. K., Chi, W. et al., Formation of DEG5 and DEG8 complexes and their involvement in the degradation of photodamaged photosystem II reaction center D1 protein in Arabidopsis. Plant Cell 2007, 19, 1347-1361.
    • (2007) Plant Cell , vol.19 , pp. 1347-1361
    • Sun, X.W.1    Peng, L.W.2    Guo, J.K.3    Chi, W.4
  • 57
    • 33745449037 scopus 로고    scopus 로고
    • LOW PSII ACCUMULATION1 is involved in efficient assembly of photosystem II in Arabidopsis thaliana
    • Zhang, L. X., Peng, L. W., Ma, J. F., Chi, W. et al., LOW PSII ACCUMULATION1 is involved in efficient assembly of photosystem II in Arabidopsis thaliana. Plant Cell 2006, 18, 955-969.
    • (2006) Plant Cell , vol.18 , pp. 955-969
    • Zhang, L.X.1    Peng, L.W.2    Ma, J.F.3    Chi, W.4
  • 58
    • 0043122986 scopus 로고    scopus 로고
    • CODEHOP (COnsensus-DEgenerate hybrid oligonucleotide primer) PCR primer design
    • Rose, T. M., Henikoff, J. G., Henikoff, S., CODEHOP (COnsensus-DEgenerate hybrid oligonucleotide primer) PCR primer design. Nucleic Acids Res. 2003, 31, 3763-3766.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3763-3766
    • Rose, T.M.1    Henikoff, J.G.2    Henikoff, S.3
  • 59
    • 38949091140 scopus 로고    scopus 로고
    • Development of an efficient protocol of RNA isolation from recalcitrant tree tissues
    • Wang, X. C., Tian, W. M., Li, Y. X., Development of an efficient protocol of RNA isolation from recalcitrant tree tissues. Mol. Biotechnol. 2008, 38, 57-64.
    • (2008) Mol. Biotechnol. , vol.38 , pp. 57-64
    • Wang, X.C.1    Tian, W.M.2    Li, Y.X.3
  • 60
    • 67449107748 scopus 로고    scopus 로고
    • Molecular cloning of oxygen-evolving enhancer genes induced by salt treatment in a halophyte, Salicornia europaea L
    • Momonoki, Y. S., Yamamoto, K., Oguri, S., Molecular cloning of oxygen-evolving enhancer genes induced by salt treatment in a halophyte, Salicornia europaea L. Plant Prod. Sci. 2009, 12, 193-198.
    • (2009) Plant Prod. Sci. , vol.12 , pp. 193-198
    • Momonoki, Y.S.1    Yamamoto, K.2    Oguri, S.3
  • 61
    • 0031452439 scopus 로고    scopus 로고
    • Protein disulfide isomerase as a regulator of chloroplast translational activation
    • Kim, J. M., Mayfield, S. P., Protein disulfide isomerase as a regulator of chloroplast translational activation. Science 1997, 278, 1954-1957.
    • (1997) Science , vol.278 , pp. 1954-1957
    • Kim, J.M.1    Mayfield, S.P.2
  • 62
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson, O., Nielsen, H., Brunak, S., von Heijne, G., Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 2000, 300, 1005-1016.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 63
    • 1842432608 scopus 로고    scopus 로고
    • The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions
    • Kleffmann, T., Russenberger, D., von Zychlinski, A., Christopher, W. et al., The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. Curr. Biol. 2004, 14, 354-362.
    • (2004) Curr. Biol. , vol.14 , pp. 354-362
    • Kleffmann, T.1    Russenberger, D.2    von Zychlinski, A.3    Christopher, W.4
  • 64
    • 33745683588 scopus 로고    scopus 로고
    • Mapping the proteome of thylakoid membranes by de novo sequencing of intermembrane peptide domains
    • Granvogl, B., Reisinger, V., Eichacker, L. A., Mapping the proteome of thylakoid membranes by de novo sequencing of intermembrane peptide domains. Proteomics 2006, 6, 3681-3695.
    • (2006) Proteomics , vol.6 , pp. 3681-3695
    • Granvogl, B.1    Reisinger, V.2    Eichacker, L.A.3
  • 65
    • 34548245076 scopus 로고    scopus 로고
    • Growth and photosynthetic responses to salinity of the salt-marsh shrub Atriplex portulacoides
    • Redondo-Gomez, S., Mateos-Naranjo, E., Davy, A. J., Fernandez-Munoz, F. et al., Growth and photosynthetic responses to salinity of the salt-marsh shrub Atriplex portulacoides. Ann. Bot. 2007, 100, 555-563.
    • (2007) Ann. Bot. , vol.100 , pp. 555-563
    • Redondo-Gomez, S.1    Mateos-Naranjo, E.2    Davy, A.J.3    Fernandez-Munoz, F.4
  • 66
    • 33747105486 scopus 로고    scopus 로고
    • Growth and photosynthetic responses to salinity in an extreme halophyte, Sarcocornia fruticosa
    • Redondo-Gomez, S., Wharmby, C., Castillo, J. M., Mateos-Naranjo, E. et al., Growth and photosynthetic responses to salinity in an extreme halophyte, Sarcocornia fruticosa. Physiol. Plant. 2006, 128, 116-124.
    • (2006) Physiol. Plant. , vol.128 , pp. 116-124
    • Redondo-Gomez, S.1    Wharmby, C.2    Castillo, J.M.3    Mateos-Naranjo, E.4
  • 67
    • 0001438597 scopus 로고
    • Stomatal and nonstomatal components to inhibition of photosynthesis in leaves of Capsicum annuum during progressive exposure to NaCl salinity
    • Bethke, P. C., Drew, M. C., Stomatal and nonstomatal components to inhibition of photosynthesis in leaves of Capsicum annuum during progressive exposure to NaCl salinity. Plant Physiol. 1992, 99, 219-226.
    • (1992) Plant Physiol. , vol.99 , pp. 219-226
    • Bethke, P.C.1    Drew, M.C.2
  • 69
    • 0242476302 scopus 로고    scopus 로고
    • Influence of salinity on photosynthesis of halophytes
    • Läuchli, A., Lüttge, U. (Eds.), Kluwer, Dordrecht, The Netherlands
    • Lovelock, C. E., Ball, M., Influence of salinity on photosynthesis of halophytes, in: Läuchli, A., Lüttge, U. (Eds.), Salinity: Environment - Plant - Molecules, 2002, Kluwer, Dordrecht, The Netherlands, pp. 315-339.
    • (2002) Salinity: Environment - Plant - Molecules , pp. 315-339
    • Lovelock, C.E.1    Ball, M.2
  • 70
    • 0030750443 scopus 로고    scopus 로고
    • Light-harvesting chlorophyll a/b-binding protein stably inserts into etioplast membranes supplemented with Zn-pheophytin a/b
    • Kuttkat, A., Edhofer, I., Eichacker, L. A., Paulsen, H., Light-harvesting chlorophyll a/b-binding protein stably inserts into etioplast membranes supplemented with Zn-pheophytin a/b. J. Biol. Chem. 1997, 272, 20451-20455.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20451-20455
    • Kuttkat, A.1    Edhofer, I.2    Eichacker, L.A.3    Paulsen, H.4
  • 71
    • 3042680691 scopus 로고    scopus 로고
    • NaCl-induced phosphorylation of light harvesting chlorophyll a/b proteins in thylakoid membranes from the halotolerant green alga, Dunaliella salina
    • Liu, X. D., Shen, Y. G., NaCl-induced phosphorylation of light harvesting chlorophyll a/b proteins in thylakoid membranes from the halotolerant green alga, Dunaliella salina. FEBS Lett. 2004, 569, 337-340.
    • (2004) FEBS Lett. , vol.569 , pp. 337-340
    • Liu, X.D.1    Shen, Y.G.2
  • 72
    • 34547666475 scopus 로고    scopus 로고
    • LPA2 is required for efficient assembly of photosystem II in Arabidopsis thaliana
    • Ma, J. F., Peng, L. W., Guo, J. K., Lu, Q. T. et al., LPA2 is required for efficient assembly of photosystem II in Arabidopsis thaliana. Plant Cell 2007, 19, 1980-1993.
    • (2007) Plant Cell , vol.19 , pp. 1980-1993
    • Ma, J.F.1    Peng, L.W.2    Guo, J.K.3    Lu, Q.T.4
  • 75
    • 44949239596 scopus 로고    scopus 로고
    • Altered photosynthetic electron channelling into cyclic electron flow and nitrite assimilation in a mutant of ferredoxin: NADPH reductase
    • Hanke, G. T., Endo, T., Satoh, F., Hase, T., Altered photosynthetic electron channelling into cyclic electron flow and nitrite assimilation in a mutant of ferredoxin: NADPH reductase. Plant Cell Environ. 2008, 31, 1017-1028.
    • (2008) Plant Cell Environ. , vol.31 , pp. 1017-1028
    • Hanke, G.T.1    Endo, T.2    Satoh, F.3    Hase, T.4
  • 77
    • 78649761413 scopus 로고    scopus 로고
    • Metabolic and signaling aspects underpinning the regulation of plant carbon nitrogen interactions
    • Nunes-Nesi, A., Fernie, A. R., Stitt, M., Metabolic and signaling aspects underpinning the regulation of plant carbon nitrogen interactions. Mol. Plant 2010, 3, 973-996.
    • (2010) Mol. Plant , vol.3 , pp. 973-996
    • Nunes-Nesi, A.1    Fernie, A.R.2    Stitt, M.3
  • 79
    • 0033895244 scopus 로고    scopus 로고
    • Enhanced tolerance to salt stress in transgenic rice that overexpresses chloroplast glutamine synthetase
    • Hoshida, H., Tanaka, Y., Hibino, T., Hayashi, Y. et al., Enhanced tolerance to salt stress in transgenic rice that overexpresses chloroplast glutamine synthetase. Plant Mol. Biol. 2000, 43, 103-111.
    • (2000) Plant Mol. Biol. , vol.43 , pp. 103-111
    • Hoshida, H.1    Tanaka, Y.2    Hibino, T.3    Hayashi, Y.4
  • 80
    • 34250807129 scopus 로고    scopus 로고
    • Tetrapyrrole biosynthesis in higher plants
    • Tanaka, R., Tanaka, A., Tetrapyrrole biosynthesis in higher plants. Annu. Rev. Plant Physiol. 2007, 58, 321-346.
    • (2007) Annu. Rev. Plant Physiol. , vol.58 , pp. 321-346
    • Tanaka, R.1    Tanaka, A.2
  • 81
    • 1842483066 scopus 로고    scopus 로고
    • PPR motifs of the nucleus-encoded factor, PGR3, function in the selective and distinct steps of chloroplast gene expression in Arabidopsis
    • Yamazaki, H., Tasaka, M., Shikanai, T., PPR motifs of the nucleus-encoded factor, PGR3, function in the selective and distinct steps of chloroplast gene expression in Arabidopsis. Plant J. 2004, 38, 152-163.
    • (2004) Plant J. , vol.38 , pp. 152-163
    • Yamazaki, H.1    Tasaka, M.2    Shikanai, T.3
  • 82
    • 60549092086 scopus 로고    scopus 로고
    • The RNA-binding proteins CSP41a and CSP41b may regulate transcription and translation of chloroplast-encoded RNAs in Arabidopsis
    • Bollenbach, T. J., Sharwood, R. E., Gutierrez, R., Lerbs-Mache, S. et al., The RNA-binding proteins CSP41a and CSP41b may regulate transcription and translation of chloroplast-encoded RNAs in Arabidopsis. Plant Mol. Biol. 2009, 69, 541-552.
    • (2009) Plant Mol. Biol. , vol.69 , pp. 541-552
    • Bollenbach, T.J.1    Sharwood, R.E.2    Gutierrez, R.3    Lerbs-Mache, S.4
  • 83
    • 4043067925 scopus 로고    scopus 로고
    • Import pathways of chloroplast interior proteins and the outer-membrane protein OEP14 converge at Toc75
    • Tu, S. L., Chen, L. J., Smith, M. D., Su, Y. S. et al., Import pathways of chloroplast interior proteins and the outer-membrane protein OEP14 converge at Toc75. Plant Cell 2004, 16, 2078-2088.
    • (2004) Plant Cell , vol.16 , pp. 2078-2088
    • Tu, S.L.1    Chen, L.J.2    Smith, M.D.3    Su, Y.S.4
  • 84
    • 33646145726 scopus 로고    scopus 로고
    • Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts
    • Adam, Z., Rudella, A., van Wijk, K. J., Recent advances in the study of Clp, FtsH and other proteases located in chloroplasts. Curr. Opin. Plant Biol. 2006, 9, 234-240.
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 234-240
    • Adam, Z.1    Rudella, A.2    van Wijk, K.J.3
  • 85
    • 0030026850 scopus 로고    scopus 로고
    • Molecular chaperones are present in the thylakoid lumen of pea chloroplasts
    • Schlicher, T., Soll, J., Molecular chaperones are present in the thylakoid lumen of pea chloroplasts. FEBS Lett. 1996, 379, 302-304.
    • (1996) FEBS Lett. , vol.379 , pp. 302-304
    • Schlicher, T.1    Soll, J.2
  • 86
    • 0026799384 scopus 로고
    • Plant organelles contain distinct peptidylprolyl cis, trans-isomerases
    • Breiman, A., Fawcett, T. W., Ghirardi, M. L., Mattoo, A. K., Plant organelles contain distinct peptidylprolyl cis, trans-isomerases. J. Biol. Chem. 1992, 267, 21293-21296.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21293-21296
    • Breiman, A.1    Fawcett, T.W.2    Ghirardi, M.L.3    Mattoo, A.K.4
  • 87
    • 49249096670 scopus 로고    scopus 로고
    • AtCYP38 ensures early biogenesis, correct assembly and sustenance of photosystem II
    • Sirpio, S., Khrouchtchova, A., Allahverdiyeva, Y., Hansson, M. et al., AtCYP38 ensures early biogenesis, correct assembly and sustenance of photosystem II. Plant J. 2008, 55, 639-651.
    • (2008) Plant J. , vol.55 , pp. 639-651
    • Sirpio, S.1    Khrouchtchova, A.2    Allahverdiyeva, Y.3    Hansson, M.4
  • 88
    • 0037795745 scopus 로고    scopus 로고
    • The oxidative pentose phosphate pathway: structure and organisation
    • Kruger, N. J., von Schaewen, A., The oxidative pentose phosphate pathway: structure and organisation. Curr. Opin. Plant Biol. 2003, 6, 236-246.
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 236-246
    • Kruger, N.J.1    von Schaewen, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.